Discovery - University of Dundee - Online Publications

Library & Learning Centre

The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin

Standard

The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin. / Chen, Shuai; Synowsky, Silvia; Tinti, Michele; MacKintosh, Carol.

In: Trends in Endocrinology and Metabolism, Vol. 22, No. 11, 11.2011, p. 429-436.

Research output: Contribution to journalScientific review

Harvard

Chen, S, Synowsky, S, Tinti, M & MacKintosh, C 2011, 'The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin' Trends in Endocrinology and Metabolism, vol 22, no. 11, pp. 429-436.

APA

Chen, S., Synowsky, S., Tinti, M., & MacKintosh, C. (2011). The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin. Trends in Endocrinology and Metabolism, 22(11), 429-436doi: 10.1016/j.tem.2011.07.005

Vancouver

Chen S, Synowsky S, Tinti M, MacKintosh C. The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin. Trends in Endocrinology and Metabolism. 2011 Nov;22(11):429-436.

Author

Chen, Shuai; Synowsky, Silvia; Tinti, Michele; MacKintosh, Carol / The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin.

In: Trends in Endocrinology and Metabolism, Vol. 22, No. 11, 11.2011, p. 429-436.

Research output: Contribution to journalScientific review

Bibtex - Download

@article{b14e1e21a3564bfc9e7a5d77d5ed4198,
title = "The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin",
author = "Shuai Chen and Silvia Synowsky and Michele Tinti and Carol MacKintosh",
year = "2011",
volume = "22",
number = "11",
pages = "429--436",
journal = "Trends in Endocrinology and Metabolism",
issn = "1043-2760",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin

A1 - Chen,Shuai

A1 - Synowsky,Silvia

A1 - Tinti,Michele

A1 - MacKintosh,Carol

AU - Chen,Shuai

AU - Synowsky,Silvia

AU - Tinti,Michele

AU - MacKintosh,Carol

PY - 2011/11

Y1 - 2011/11

N2 - <p>How does signalling via PI3K-PKB (AKT)-mTORC1-p70S6K and ERK-p90RSK mediate wide-ranging physiological responses to insulin? Quantitative proteomics and biochemical experiments are revealing that these signalling pathways induce the phosphorylation of large and overlapping sets of proteins, which are then captured by phosphoprotein-binding proteins named 14-3-3 s. The 14-3-3 s are dimers; that dock onto dual-phosphorylated sites in a configuration with special signalling and mechanical properties. They interact with the Rab GTPase-activating proteins AS160 and TBC1D1 to regulate glucose uptake into target tissues in response to insulin and energy stress. Dynamic patterns in the 14-3-3-binding phosphoproteome are providing new insights into how insulin triggers coherent shifts in metabolism that are integrated with other cellular response systems.</p>

AB - <p>How does signalling via PI3K-PKB (AKT)-mTORC1-p70S6K and ERK-p90RSK mediate wide-ranging physiological responses to insulin? Quantitative proteomics and biochemical experiments are revealing that these signalling pathways induce the phosphorylation of large and overlapping sets of proteins, which are then captured by phosphoprotein-binding proteins named 14-3-3 s. The 14-3-3 s are dimers; that dock onto dual-phosphorylated sites in a configuration with special signalling and mechanical properties. They interact with the Rab GTPase-activating proteins AS160 and TBC1D1 to regulate glucose uptake into target tissues in response to insulin and energy stress. Dynamic patterns in the 14-3-3-binding phosphoproteome are providing new insights into how insulin triggers coherent shifts in metabolism that are integrated with other cellular response systems.</p>

U2 - 10.1016/j.tem.2011.07.005

DO - 10.1016/j.tem.2011.07.005

M1 - Scientific review

JO - Trends in Endocrinology and Metabolism

JF - Trends in Endocrinology and Metabolism

SN - 1043-2760

IS - 11

VL - 22

SP - 429

EP - 436

ER -

Documents

Library & Learning Centre

Contact | Accessibility | Policy